The integrin family of transmembrane receptors have long been recognized for their structural roles in linking extracellular matrix proteins with the cellular actin cytoskeleton to regulate cell shape, cell migration and tissue architecture. Lately, it has become clear that integrin receptors can initiate intracellular signals that synergize with those from growth-factor receptor protein-tyrosine kinases in modulating cell growth. This review describes our current knowledge of integrin-stimulated tyrosine phosphorylation events and downstream signalling pathways, with emphasis on the recent progress made in understanding the molecular pathways linking the integrin receptors with mitogen-activated protein (MAP) kinase cascades.